Fig. 4: Crystal structure of TEX12 FFV in a dimeric conformation.
From: Coiled-coil structure of meiosis protein TEX12 and conformational regulation by its C-terminal tip
a Crystal structure of a TEX12 FFV dimer. The two TEX12 chains (coloured blue to red in an N- to C-terminal direction) are arranged in an anti-parallel configuration such that their Ctip sequences project from either side of the core dimer, formed of amino-acids 49–113, to form a 130 Å molecule. b The dimeric core is formed of two anti-parallel coiled-coils with a midline six amino-acid insertion, forming a central hinge of R78-D82 salt bridges that act as struts to locally separate the interacting chains. c Superposition of the TEX12 FFV dimer structure (blue) and a constituent dimer of the TEX12 ΔCtip structure (yellow), demonstrating their shared hinge and dimer interface (r.m.s. deviation of 1.11). d, e The TEX12 FFV crystal lattice includes (d) end-on dimer-of-dimers assembly through formation of anti-parallel coiled-coils between Ctip sequences, which (e) interact with the Ctip ends of two additional molecules within anti-parallel Ctip tetrameric assemblies.
